Cited by 242Cellular transport and secretionEndoplasmic Reticulum Stress and DiseaseIon Channels and Receptors

Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis

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Müller‐Taubenberger, Annette, Lupas, Andrei N, Li, Hewang, Ecke, Mary, Simmeth, Evelyn, Gerisch, Günther·2001·The EMBO Journal

Abstract

Calreticulin and calnexin are Ca2+-binding proteins with chaperone activity in the endoplasmic reticulum. These proteins have been eliminated by gene replacement in Dictyostelium, the only microorganism known to harbor both proteins; family members in Dictyostelium are located at the base of phylogenetic trees. A dramatic decline in the rate of phagocytosis was observed in double mutants lacking calreticulin and calnexin, whereas only mild changes occurred in single mutants. Dictyostelium cells are professional phagocytes, capable of internalizing particles by a sequence of activities: adhesion of the particle to the cell surface, actin-dependent outgrowth of a phagocytic cup, and separation of the phagosome from the plasma membrane. In the double-null mutants, particles still adhered to the cell surface, but the outgrowth of phagocytic cups was compromised. Green fluorescent protein-tagged calreticulin and calnexin, expressed in wild-type cells, revealed a direct link of the endoplasmic reticulum to the phagocytic cup enclosing a particle, such that the Ca2+ storage capacity of calreticulin and calnexin might directly modulate activities of the actin system during particle uptake.

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Crossref · 10.1093/emboj/20.23.6772

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  • V-H+ ATPase, Rab7 and calreticulin are typical markers of phagosomal traffic, whereas gp24, discoidin II and gp130 are extracellular or membrane proteins that could be entrapped in the phagosome.

    “The V-H+ ATPase, Rab7 and calreticulin are typical markers of phagosomal traffic [16,81-83], whereas gp24, discoidin II and gp130 are extracellular or membrane proteins that could be entrapped in the phagosome.”

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Authors
Müller‐Taubenberger, A., Lupas, A. N., Li, H., Ecke, M., Simmeth, E., & Gerisch, G.
Affiliations
  • Max Planck Institute of Biochemistry (DE)
  • Max Planck Institute for Developmental Biology (DE)
Corresponding author
Gerisch, Günther
Venue
The EMBO Journal
Published
2001-12-03
Volume
20
Issue
23
Pages
6772-6782
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W2003650736
Cited by
242
References
2
Citations by year
2026: 7 · 2025: 6 · 2024: 7 · 2023: 6 · 2022: 8 · 2021: 12 · 2020: 12 · 2019: 8 · 2018: 12 · 2017: 7 · 2016: 6 · 2015: 3 · 2014: 11 · 2013: 5 · 2012: 14
FWCI
3.63
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
Deutsche Forschungsgemeinschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
calreticulin, calnexin, phagocytosis, endoplasmic reticulum, Dictyostelium, calcium-binding proteins, molecular chaperones, phagocytic cup, phagosome formation, calcium storage, gene replacement mutants
MeSH terms
Animals, Calcium, Calcium-Binding Proteins, Cell Adhesion, Chemotaxis, Dictyostelium, Endoplasmic Reticulum, Genetic Vectors, Luminescent Proteins, Mice, Inbred BALB C, Microscopy, Fluorescence, Models, Genetic, Mutation, Phagocytosis, Phylogeny, Protein Binding, Recombinant Fusion Proteins, Ribonucleoproteins, Time Factors, Transformation, Genetic, Blotting, Southern, Protein Structure, Tertiary, DNA, Complementary, Animals, Genetically Modified, Calnexin, Calreticulin, Green Fluorescent Proteins, Mice

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